Disease relevance of tuf

• EF-Tu is highly conserved in all bacteria and is known to be N-acetylated in Escherichia coli [1].
• A feature that is common to both bacteria and to Thermoanaerobacterium sp. appears to be that the lining and the fibrils crossing the cytoplasm contain a high number of copies of the bacterial elongation factor Tu (EF-Tu) [2].

High impact information on tuf

• The N terminus of bacterial elongation factor Tu elicits innate immunity in Arabidopsis plants [1].
• The shorter peptide, elf12, comprising the acetyl group and the first 12 N-terminal amino acids, is inactive as elicitor but acts as a specific antagonist for EF-Tu-related elicitors [1].
• The mutations had no effect on EF-Tu-dependent delivery of aminoacyl-tRNA to the ribosome [3].
• An important feature of the nucleotide exchange is the structural rearrangement of EF-Tu in the EF-Tu.EF-Ts complex caused by insertion of Phe-81 of EF-Ts between His-84 and His-118 of EF-Tu [3].
• The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange [3].

Anatomical context of tuf

• Current research and developmental efforts are aimed at the design of a new class of antibacterial drugs, acting by destabilization of the EF-Tu-containing bacterial cytoskeleton, and of an innovative mode of inducible lysis of recombinant bacteria by controlled destabilization of the EF-Tu-containing cytoskeleton [2].

References